Crystallization and preliminary x-ray diffraction study of synthetic apolipoprotein E fragment (residues 129-169).
Apolipoprotein E is a plasma protein comprised of a lipid binding region (which together with other apoproteins maintains the structure of lipoprotein particles) and a receptor binding domain (which interacts with cellular receptors for control of triglyceride and cholesterol metabolism). A peptide, comprising residues 129-169 of human apolipoprotein E, which contains both a putative lipid-binding region and receptor binding domain, has been synthesized by solid phase techniques. Diffraction quality crystals of the synthetic apolipoprotein E fragment129-169 have been obtained at room temperature by vapor diffusion with polyethylene glycol in the presence of the nonionic detergent beta-octylglucoside. The crystals have been characterized with x-radiation as orthorhombic, space group I222 or I2(1)2(1)2(1), with unit cell dimensions a = 61.91, b = 30.84, and c = 42.79 A. There are eight molecules per unit cell, with one molecule (Mr = 4771) in each asymmetric unit. Precession photographs show that crystals diffract beyond 2.7-A resolution and are stable in the x-ray beam at room temperature for at least 200 h; thus, they can be used to collect three-dimensional data for a detailed crystallographic analysis.
Maulik
P R
PR
Biophysics Department, Housman Medical Research Center, Boston University School of Medicine, Massachusetts 02118.
Reed
R A
RA
Sparrow
D A
DA
Sparrow
J T
JT
Shipley
G G
GG
D001057:Apolipoproteins E / Q000138:chemical synthesis*; D003460:Crystallization; D005960:Glucosides; D006801:Humans; D010446:Peptide Fragments / Q000138:chemical synthesis*; D011092:Polyethylene Glycols; D014961:X-Ray Diffraction
D001057:Apolipoproteins E; D005960:Glucosides; D010446:Peptide Fragments; C018619:octyl-beta-D-glucoside; D011092:Polyethylene Glycols